STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CN09_27610Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology (206 aa)    
Predicted Functional Partners:
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity
  
 0.988
dnaK
Molecular chaperone dnak; Acts as a chaperone
  
 0.983
CN09_34040
Molecular chaperone dnak; Acts as a chaperone
  
 0.983
CN09_11775
Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family
  
 0.982
fusA
Elongation factor g; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome
  
 0.979
groL
Molecular chaperone groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions
  
 0.971
CN09_27060
Molecular chaperone groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions
  
 0.971
CN09_01625
GlcNAc transferase; Derived by automated computational analysis using gene prediction method: Protein Homology
 
 0.965
CN09_02050
Hypothetical protein; Uncharacterized protein; Derived by automated computational analysis using gene prediction method: Protein Homology
 
 0.965
atpE
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation
 
  
 0.965
Your Current Organism:
Agrobacterium rhizogenes
NCBI taxonomy Id: 359
Other names: A. rhizogenes, ATCC 11325, Agrobacterium biovar 2, Agrobacterium genomic group 10, Agrobacterium genomic species 10, Agrobacterium genomosp. 10, Agrobacterium rhizogenes (RI plasmid PRI1724), Agrobacterium rhizogenes (RI plasmid PRI8196), Agrobacterium rhizogenes (RI plasmid PRIA4B), CFBP 5520, CIP 104328, DSM 30148, ICMP 5794, IFO 13257, JCM 20919, LMG 150, NBRC 13257, NCPPB 2991, Rhizobium rhizogenes, Rhizobium sp. LMG 9509
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